QSOX1_ORYSJ
ID QSOX1_ORYSJ Reviewed; 513 AA.
AC Q6AUC6; A0A0P0WQM2; Q0DG53;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sulfhydryl oxidase 1;
DE EC=1.8.3.2;
DE AltName: Full=Quiescin-sulfhydryl oxidase 1;
DE Short=OsQSOX1;
DE Flags: Precursor;
GN Name=QSOX1; OrderedLocusNames=Os05g0552500, LOC_Os05g47930;
GN ORFNames=OsJ_19470, OSJNBa0079H23.16;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC protein thiols to disulfides with the reduction of oxygen to hydrogen
CC peroxide. May contribute to disulfide bond formation in a variety of
CC secreted proteins (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00654};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF18170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC129717; AAT85195.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18170.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014961; BAS95229.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64618.1; -; Genomic_DNA.
DR EMBL; AK121660; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015640480.1; XM_015784994.1.
DR AlphaFoldDB; Q6AUC6; -.
DR SMR; Q6AUC6; -.
DR STRING; 4530.OS05T0552500-02; -.
DR PaxDb; Q6AUC6; -.
DR PRIDE; Q6AUC6; -.
DR EnsemblPlants; Os05t0552500-02; Os05t0552500-02; Os05g0552500.
DR GeneID; 4339541; -.
DR Gramene; Os05t0552500-02; Os05t0552500-02; Os05g0552500.
DR KEGG; osa:4339541; -.
DR eggNOG; KOG1731; Eukaryota.
DR HOGENOM; CLU_041851_0_0_1; -.
DR InParanoid; Q6AUC6; -.
DR OMA; FASAKWD; -.
DR OrthoDB; 498515at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q6AUC6; baseline and differential.
DR Genevisible; Q6AUC6; OS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; PTHR22897; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; FAD; Flavoprotein; Glycoprotein; Oxidoreductase;
KW Redox-active center; Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..513
FT /note="Sulfhydryl oxidase 1"
FT /id="PRO_0000400052"
FT DOMAIN 31..174
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 304..406
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 320
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 377..384
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..79
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 301..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 348..351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 412..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT CONFLICT 160
FT /note="R -> G (in Ref. 6; AK121660)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="S -> G (in Ref. 6; AK121660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57849 MW; B891D5944EDC38A4 CRC64;
MAAAAVARRV VLVLVLAAAS LAAAPRGAAA RSLGGREGPG EVDADAAVDL NATNFDAFLK
ASLEPWAVVE FFAHWCPACR NYKPHYEKVA KLFNGRDAAH PGLILMARVD CASKVNIDLC
NRFSVDHYPF LLWGPPTKFA SAKWDPKQEN NEIKLIDDGR TAERLLKWIN NQMKSSFSLE
DKKYENENML PKNASDPEQI VQAIYDVEEA TAQALQIILE RKTIKPKNRD SLIRFLQILV
ARHPSKRCRR GSAELLINFD DHWSSNLSLS SQEGSKLLES VAEENHWICG KEVPRGYWLF
CRGSKSETRG FSCGLWVLMH SLTVRIGDGE SQSTFTSICD FIHNFFICEE CRKHFYEMCS
SVSAPFRTAR ELSLWLWSTH NKVNMRLMKE EKDMGTGDPL FPKVTWPPNQ LCPSCYRSSK
VTDGAVDWNE DAVYQFLVNY YGKKLVSSYK ETYMESLQQQ EKKIVSEDSS ISNAASVPIG
AALGVAIASC TFGALACFWR AQQKNRKQRK NWN
